inhibits antigen-mediated Syk, but not Lyn tyrosine kinase activation in mast cells
- 2 January 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 357 (1) , 41-44
- https://doi.org/10.1016/0014-5793(94)01329-y
Abstract
High affinity IgE receptors (αβγ 2) mediate the activation of the non-receptor tyrosine kinases Lyn and Syk. Here we show that the antioxidant drug (NAC) inhibits antigen-mediated Syk activation whereas Lyn activation and phosphorylation of β and γ is maintained. Furthermore, NAC inhibits antigen-mediated calcium mobilization and exocytosis in a dose-dependent manner, but does not inhibit ionomycin-induced exocytosis. These data support a model in which the activation of Lyn is responsible for receptor phosphorylation and precedes the activation of Syk. The inhibition of Syk activation by NAC may be relevant to B and T cell antigen receptors, which are also linked to Syk/ZAP70 tyrosine kinases.
Keywords
This publication has 16 references indexed in Scilit:
- Bcl-2 functions in an antioxidant pathway to prevent apoptosisCell, 1993
- Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate In vitroBiochemical and Biophysical Research Communications, 1992
- Tyrosine phosphorylation of phospholipase C γ1 couples the FCη receptor mediated signal to mast cells secretionInternational Immunology, 1992
- Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifsNature, 1992
- Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinasesNature, 1992
- Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane EnzymesScience, 1991
- PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254Cell, 1991
- Increase of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine PhosphorylationScience, 1990
- T Cell Antigen Receptor-Mediated Activation of Phospholipase C Requires Tyrosine PhosphorylationScience, 1990
- Studies with a monoclonal antibody to the β subunit of the receptor with high affinity for immunoglobulin EMolecular Immunology, 1988